A0A926M6H3 · A0A926M6H3_9PROT
- ProteinCoenzyme A biosynthesis bifunctional protein CoaBC
- GenecoaBC
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids399 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine.
Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine.
Catalytic activity
- (R)-4'-phosphopantothenate + CTP + L-cysteine = CMP + diphosphate + H+ + N-[(R)-4-phosphopantothenoyl]-L-cysteine
Cofactor
Protein has several cofactor binding sites:
Note: Binds 1 FMN per subunit.
Pathway
Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5.
Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 3/5.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 157 | Proton donor | ||||
Sequence: C | ||||||
Binding site | 279 | CTP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 289 | CTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 305-308 | CTP (UniProtKB | ChEBI) | ||||
Sequence: PDIL | ||||||
Binding site | 325 | CTP (UniProtKB | ChEBI) | ||||
Sequence: F | ||||||
Binding site | 339 | CTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 343 | CTP (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | phosphopantothenoylcysteine decarboxylase complex | |
Molecular Function | FMN binding | |
Molecular Function | metal ion binding | |
Molecular Function | phosphopantothenate--cysteine ligase activity | |
Molecular Function | phosphopantothenoylcysteine decarboxylase activity | |
Biological Process | coenzyme A biosynthetic process | |
Biological Process | pantothenate catabolic process |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameCoenzyme A biosynthesis bifunctional protein CoaBC
- Alternative names
Including 2 domains:
- Recommended namePhosphopantothenoylcysteine decarboxylase
- EC number
- Short namesPPC decarboxylase ; PPC-DC
- Alternative names
- Recommended namePhosphopantothenate--cysteine ligase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Candidatus Pelagibacterales
Accessions
- Primary accessionA0A926M6H3
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Structure
Family & Domains
Features
Showing features for region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-191 | Phosphopantothenoylcysteine decarboxylase | ||||
Sequence: MNKSKKVLLIITGGIAAYKSLEIIRGLKANNIDVTCILTKSGSEFVTPLSIESLSENKVYTDLFNLTDEHEMGHIQLSRQADVILVAPATANIMSKIAYGNTDDLASTVLVATNKPIIVAPAMNVRMWLNNATQRNIQTLRNDGIKFVGPENGEMACGEYGEGRMSEPSEIIKYTNDFINSLDFKPLRDFS | ||||||
Domain | 5-176 | Flavoprotein | ||||
Sequence: KKVLLIITGGIAAYKSLEIIRGLKANNIDVTCILTKSGSEFVTPLSIESLSENKVYTDLFNLTDEHEMGHIQLSRQADVILVAPATANIMSKIAYGNTDDLASTVLVATNKPIIVAPAMNVRMWLNNATQRNIQTLRNDGIKFVGPENGEMACGEYGEGRMSEPSEIIKYTN | ||||||
Domain | 191-369 | DNA/pantothenate metabolism flavoprotein C-terminal | ||||
Sequence: SALVTSGPTKEMIDPVRFISNESSGKQGFTIAEKLSSLGAYTTLISGPTKLPNPNVDKVVHVSSADEMMLECDKALPVNIAICAAAVADYKVMKQSETKIKKNGSRLDITLEENPDILSRLSKRNDKRPGLVVGFAAETEKLEENSKIKLEKKGCDWILGNNVSNGQVIGKDTNEIHFI | ||||||
Region | 192-399 | Phosphopantothenate--cysteine ligase | ||||
Sequence: ALVTSGPTKEMIDPVRFISNESSGKQGFTIAEKLSSLGAYTTLISGPTKLPNPNVDKVVHVSSADEMMLECDKALPVNIAICAAAVADYKVMKQSETKIKKNGSRLDITLEENPDILSRLSKRNDKRPGLVVGFAAETEKLEENSKIKLEKKGCDWILGNNVSNGQVIGKDTNEIHFISKSETENWKQMRKEEVAEKLSHKIVQHLKS |
Sequence similarities
In the C-terminal section; belongs to the PPC synthetase family.
In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length399
- Mass (Da)43,960
- Last updated2023-02-22 v1
- Checksum2AFD8521889622CA
Keywords
- Technical term